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Article ; Online: Ferroptosis Inhibitors Suppress Prostaglandin Synthesis in Lipopolysaccharide-Stimulated Macrophages.

Aleem, Ansari M / Kang, Weixi / Lin, Shuyang / Milad, Matthew / Kingsley, Philip J / Crews, Brenda C / Uddin, Md Jashim / Rouzer, Carol A / Marnett, Lawrence J

ACS chemical biology

2023 Volume 18, Issue 2, Page(s) 404–418

Abstract: Necrostatin-1 blocks ferroptosis via an unknown mechanism and necroptosis through inhibition of receptor-interacting protein kinase-1 (RIP1). We report that necrostatin-1 suppresses cyclooxygenase-2-dependent prostaglandin biosynthesis in ... ...

Abstract	Necrostatin-1 blocks ferroptosis via an unknown mechanism and necroptosis through inhibition of receptor-interacting protein kinase-1 (RIP1). We report that necrostatin-1 suppresses cyclooxygenase-2-dependent prostaglandin biosynthesis in lipopolysaccharide-treated RAW264.7 macrophages (IC
MeSH term(s)	Cyclooxygenase 2 ; Lipopolysaccharides/pharmacology ; Ferroptosis ; Peroxidases/metabolism ; Hydrogen Peroxide/metabolism ; Prostaglandins ; Macrophages/metabolism
Chemical Substances	Cyclooxygenase 2 (EC 1.14.99.1) ; Lipopolysaccharides ; Peroxidases (EC 1.11.1.-) ; Hydrogen Peroxide (BBX060AN9V) ; Prostaglandins
Language	English
Publishing date	2023-01-13
Publishing country	United States
Document type	Journal Article
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.2c00869
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Status of trace elements and antioxidants in premenopausal and postmenopausal phase of life: a comparative study.

Ansar, Sabah / Alhefdhi, Tayef / Aleem, Ansari M

International journal of clinical and experimental medicine

2015 Volume 8, Issue 10, Page(s) 19486–19490

Abstract: The aim of the study was to determine the extent of free radical damage in the form of oxidative stress, the antioxidant status and correlate with trace element levels in postmenopausal females as compared to premenopausal females. Participants between ... ...

Abstract	The aim of the study was to determine the extent of free radical damage in the form of oxidative stress, the antioxidant status and correlate with trace element levels in postmenopausal females as compared to premenopausal females. Participants between the ages of 30-60 years were recruited for the study and status of antioxidant enzymes and trace metals level was determined. The serum Calcium (Ca) levels after menopause was higher than that of the premenopausal group (P<0.001). The changes in copper (Cu) and Zinc (Zn) between the groups were not significant (p>0.05). In postmenopausal women, antioxidant enzymes like superoxide dismutase (SOD) and glutathione peroxidase (GPX), catalase (CAT) significantly decreased (P<0.001) in postmenopausal women showing oxidative stress in the cells. Concentrations of vitamin-C pointed out a significant decrease (P<0.05) in postmenopausal women when compared with premenopausal women.
Language	English
Publishing date	2015-10-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2418305-2
ISSN	1940-5901
ISSN	1940-5901
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Article: Harmaline Analogs as Substrate-Selective Cyclooxygenase-2 Inhibitors.

Uddin, Md Jashim / Xu, Shu / Crews, Brenda C / Aleem, Ansari M / Ghebreselasie, Kebreab / Banerjee, Surajit / Marnett, Lawrence J

ACS medicinal chemistry letters

2020 Volume 11, Issue 10, Page(s) 1881–1885

Abstract: We report the design, synthesis, and evaluation of a series of harmaline analogs as selective inhibitors of 2-arachidonylglycerol (2-AG) oxygenation over arachidonic acid (AA) oxygenation by purified cyclooxygenase-2 (COX-2). A fused tricyclic harmaline ... ...

Abstract	We report the design, synthesis, and evaluation of a series of harmaline analogs as selective inhibitors of 2-arachidonylglycerol (2-AG) oxygenation over arachidonic acid (AA) oxygenation by purified cyclooxygenase-2 (COX-2). A fused tricyclic harmaline analog containing a CH
Language	English
Publishing date	2020-02-14
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.9b00555
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Article ; Online: Discovery of a Redox-Activatable Chemical Probe for Detection of Cyclooxygenase-2 in Cells and Animals.

Uddin, Md Jashim / Lo, Justin Han-Je / Oltman, Connor G / Crews, Brenda C / Huda, Tamanna / Liu, Justin / Kingsley, Philip J / Lin, Shuyang / Milad, Mathew / Aleem, Ansari M / Asaduzzaman, Abu / McIntyre, J Oliver / Duvall, Craig L / Marnett, Lawrence J

ACS chemical biology

2022 Volume 17, Issue 7, Page(s) 1714–1722

Abstract: Cyclooxygenase-2 (COX-2) expression is up-regulated in inflammatory tissues and many premalignant and malignant tumors. Assessment of COX-2 protein in vivo, therefore, promises to be a powerful strategy to distinguish pathologic cells from normal cells ... ...

Abstract	Cyclooxygenase-2 (COX-2) expression is up-regulated in inflammatory tissues and many premalignant and malignant tumors. Assessment of COX-2 protein in vivo, therefore, promises to be a powerful strategy to distinguish pathologic cells from normal cells in a complex disease setting. Herein, we report the first redox-activatable COX-2 probe, fluorocoxib Q (FQ), for in vivo molecular imaging of pathogenesis. FQ inhibits COX-2 selectively in purified enzyme and cell-based assays. FQ exhibits extremely low fluorescence and displays time- and concentration-dependent fluorescence enhancement upon exposure to a redox environment. FQ enters the cells freely and binds to the COX-2 enzyme. FQ exhibits high circulation half-life and metabolic stability sufficient for target site accumulation and demonstrates COX-2-targeted uptake and retention in cancer cells and pathologic tissues. Once taken up, it undergoes redox-mediated transformation into a fluorescent compound fluorocoxib Q-H that results in high signal-to-noise contrast and differentiates pathologic tissues from non-pathologic tissues for real-time in vivo imaging.
MeSH term(s)	Animals ; Cyclooxygenase 2/metabolism ; Cyclooxygenase 2 Inhibitors/pharmacology ; Fluorescent Dyes/chemistry ; Neoplasms ; Oxidation-Reduction
Chemical Substances	Cyclooxygenase 2 Inhibitors ; Fluorescent Dyes ; Cyclooxygenase 2 (EC 1.14.99.1)
Language	English
Publishing date	2022-07-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.1c00961
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Article ; Online: Docking and mutagenesis studies lead to improved inhibitor development of ML355 for human platelet 12-lipoxygenase.

Tsai, Wan-Chen / Aleem, Ansari M / Tena, Jennyfer / Rivera-Velazquez, Mirella / Brah, Harman Singh / Tripathi, Sarvind / D'silva, Melinee / Nadler, Jerry L / Kalyanaraman, Chakrapani / Jacobson, Matthew P / Holman, Theodore

Bioorganic & medicinal chemistry

2021 Volume 46, Page(s) 116347

Abstract: Human platelet 12-(S)-Lipoxygenase (12-LOX) is a fatty acid metabolizing oxygenase that plays an important role in platelet activation and cardiometabolic disease. ML355 is a specific 12-LOX inhibitor that has been shown to decrease thrombosis without ... ...

Abstract	Human platelet 12-(S)-Lipoxygenase (12-LOX) is a fatty acid metabolizing oxygenase that plays an important role in platelet activation and cardiometabolic disease. ML355 is a specific 12-LOX inhibitor that has been shown to decrease thrombosis without prolonging hemostasis and protect human pancreatic islets from inflammatory injury. It has an amenable drug-like scaffold with nM potency and encouraging ADME and PK profiles, but its binding mode to the active site of 12-LOX remains unclear. In the current work, we combined computational modeling and experimental mutagenesis to propose a model in which ML355 conforms to the "U" shape of the 12-LOX active site, with the phenyl linker region wrapping around L407. The benzothiazole of ML355 extends into the bottom of the active site cavity, pointing towards residues A417 and V418. However, reducing the active site depth alone did not affect ML355 potency. In order to lower the potency of ML355, the cavity needed to be reduced in both length and width. In addition, H596 appears to position ML355 in the active site through an interaction with the 2-methoxy phenol moiety of ML355. Combined, this binding model suggested that the benzothiazole of ML355 could be enlarged. Therefore, a naphthyl-benzothiazole derivative of ML355, Lox12Slug001, was synthesized and shown to have 7.2-fold greater potency than ML355. This greater potency is proposed to be due to additional van der Waals interactions and pi-pi stacking with F414 and F352. Lox12Slug001 was also shown to be highly selective against 12-LOX relative to the other LOX isozymes and more importantly, it showed activity in rescuing human islets exposed to inflammatory cytokines with comparable potency to ML355. Further studies are currently being pursued to derivatize ML355 in order to optimize the additional space in the active site, while maintaining acceptable drug-like properties.
MeSH term(s)	Arachidonate 12-Lipoxygenase/metabolism ; Dose-Response Relationship, Drug ; Drug Development ; Humans ; Lipoxygenase Inhibitors/chemical synthesis ; Lipoxygenase Inhibitors/chemistry ; Lipoxygenase Inhibitors/pharmacology ; Molecular Docking Simulation ; Molecular Structure ; Structure-Activity Relationship ; Sulfonamides/chemical synthesis ; Sulfonamides/chemistry ; Sulfonamides/pharmacology
Chemical Substances	Lipoxygenase Inhibitors ; ML355 ; Sulfonamides ; Arachidonate 12-Lipoxygenase (EC 1.13.11.31)
Language	English
Publishing date	2021-08-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2021.116347
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Zs.A 3815: Show issues

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Article: Targeted Detection of Cyclooxygenase-1 in Ovarian Cancer.

Malerba, Paola / Crews, Brenda C / Ghebreselasie, Kebreab / Daniel, Cristina K / Jashim, Elma / Aleem, Ansari M / Salam, Redoan A / Marnett, Lawrence J / Uddin, Md Jashim

ACS medicinal chemistry letters

2019 Volume 11, Issue 10, Page(s) 1837–1842

Abstract: Overexpression of cyclooxygenase-1 (COX-1) is associated with the initiation and progression of ovarian cancer, and targeted imaging of COX-1 is a promising strategy for early detection of this disease. We report the discovery ... ...

Abstract	Overexpression of cyclooxygenase-1 (COX-1) is associated with the initiation and progression of ovarian cancer, and targeted imaging of COX-1 is a promising strategy for early detection of this disease. We report the discovery of
Language	English
Publishing date	2019-07-24
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.9b00280
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Article ; Online: Targeting COX-1 by mofezolac-based fluorescent probes for ovarian cancer detection.

Scilimati, Antonio / Ferorelli, Savina / Iaselli, Maria Clara / Miciaccia, Morena / Pati, Maria Laura / Fortuna, Cosimo G / Aleem, Ansari M / Marnett, Lawrence J / Perrone, Maria Grazia

European journal of medicinal chemistry

2019 Volume 179, Page(s) 16–25

Abstract: Biomarkers of specific targets are becoming an essential objective for clinical unmet clinical needs to improve diseases early detection and increase patient overall survival. Ovarian cancer is among the highest mortality gynecological cancers. It is ... ...

Abstract	Biomarkers of specific targets are becoming an essential objective for clinical unmet clinical needs to improve diseases early detection and increase patient overall survival. Ovarian cancer is among the highest mortality gynecological cancers. It is asymptomatic and almost always diagnosed at advanced stage. At five years from the first diagnosis the survival rate of ovarian cancer patients is only 30%. Cyclooxygenase (COX)-1 as opposed to COX-2 is known to be overexpressed in ovarian cancer. Therefore, fluorescent probes targeting COX-1 were designed and prepared in fair to good yields for its quantitatively detection in human ovarian cancer cell lines (OVCAR-3 and SKOV-3). In particular, both cytofluorimetric and immunofluorescent experiments showed that N-[4-(9-dimethylimino-9H-benzo[a]phenoxazin-5-ylamino)butyl]-2-(3,4-bis(4-methoxyphenyl)isoxazol-5-yl)acetamide chloride (11) enters into OVCAR-3 cells and is mainly localized on the membrane containing the COX-1. Membrane fluorescence emission represents about 80% of the total fluorescence measured in the whole cell, while the non-specific labeling represents only 20%. This result indicates that the intensity of fluorescence emission is almost exclusively attributable to 11 bound to COX-1 located on the membrane. Furthermore, no diffusion inside the cell occurs. IC
MeSH term(s)	Cell Line, Tumor ; Cyclooxygenase 1/metabolism ; Cyclooxygenase Inhibitors/chemical synthesis ; Cyclooxygenase Inhibitors/chemistry ; Cyclooxygenase Inhibitors/pharmacology ; Dose-Response Relationship, Drug ; Female ; Fluorescent Dyes/chemical synthesis ; Fluorescent Dyes/chemistry ; Fluorescent Dyes/pharmacology ; HEK293 Cells ; Humans ; Isoxazoles/chemical synthesis ; Isoxazoles/chemistry ; Isoxazoles/pharmacology ; Molecular Structure ; Optical Imaging ; Ovarian Neoplasms/diagnostic imaging ; Structure-Activity Relationship
Chemical Substances	Cyclooxygenase Inhibitors ; Fluorescent Dyes ; Isoxazoles ; Cyclooxygenase 1 (EC 1.14.99.1) ; PTGS1 protein, human (EC 1.14.99.1) ; mofezolac (RVJ0BV3H3Y)
Language	English
Publishing date	2019-06-15
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2019.06.039
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Zs.B 784: Show issues

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Article: Molecular Imaging of Inflammation in Osteoarthritis Using a Water-Soluble Fluorocoxib.

Uddin, Md Jashim / Vemulapalli, Anoop / Niitsu, Hiroaki / Crews, Brenda C / Oltman, Connor G / Kingsley, Philip J / Kavanaugh, Taylor E / Bedingfield, Sean K / Mcintyre, J Oliver / Milad, Matthew / Aleem, Ansari M / Coffey, Robert J / Duvall, Craig L / Marnett, Lawrence J

ACS medicinal chemistry letters

2020 Volume 11, Issue 10, Page(s) 1875–1880

Abstract: Clinical imaging approaches to detect inflammatory biomarkers, such as cyclooxygenase-2 (COX-2), may facilitate the diagnosis and therapy of inflammatory diseases. To this end, we report the discovery ... ...

Abstract	Clinical imaging approaches to detect inflammatory biomarkers, such as cyclooxygenase-2 (COX-2), may facilitate the diagnosis and therapy of inflammatory diseases. To this end, we report the discovery of
Language	English
Publishing date	2020-02-24
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.9b00512
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Article: VLHL plasminogen activator inhibitor spontaneously reactivates from the latent to active form.

Jankun, Jerzy / Aleem, Ansari M / Selman, Steve H / Basrur, Venkatesha / Skrzypczak-Jankun, Ewa

International journal of molecular medicine

2009 Volume 23, Issue 1, Page(s) 57–63

Abstract: Wild-type plasminogen activator inhibitor type 1 (PAI-1) is a fast-acting uPA and tPA inhibitor with half-life of 1-2 h. Recombinant PAI-1 with two mutations, Q197C and G355C, shows a very long half-life (VLHL). An introduced disulfide bridge holds ... ...

Abstract	Wild-type plasminogen activator inhibitor type 1 (PAI-1) is a fast-acting uPA and tPA inhibitor with half-life of 1-2 h. Recombinant PAI-1 with two mutations, Q197C and G355C, shows a very long half-life (VLHL). An introduced disulfide bridge holds together two central, parallel strands of beta-sheet A, preventing their separation to incorporate residues P4-P14 during the serpin's transition into latency. An active PAI-1 is usually described as a single structure with the reactive center loop (RCL) with P1-P1' (R369-M370) extended far from the bulk of the serpin's body. We have found that VLHL PAI-1 exists in several active forms that travel with different electrophoretic mobilities. Under aerobic conditions, two distinct active forms are observed. Upon reduction of cysteines, the VLHL mutant converts into the latent form, which spontaneously reactivates into a fully or partially active serpin, with yet another mobility. Utilizing electrophoresis, zymography (to check PAI-1 activity toward uPA) and theoretical calculations for molecular modeling, we have characterized active 1, 2, 3 and latent conformers of VLHL PAI-1 and their behaviors at normal and elevated temperatures, and in normal or reducing environments. VLHL PAI-1 activity is not affected, and the molecules do not polymerize unless reduced and/or heated. VLHL PAI-1 associates into dimers and bigger oligomers when -SH groups become available for oxidation and formation of intra- or intermolecular -S-S- bridges between conformers of different shapes and activities. We postulate that the active structures differ in RCL conformation and their position in relation to the gate region and the rest of the molecule.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Catalytic Domain ; Chromatography, Liquid ; Half-Life ; Hot Temperature ; Humans ; Plasminogen Activator Inhibitor 1/chemistry ; Plasminogen Activator Inhibitor 1/genetics ; Plasminogen Activator Inhibitor 1/isolation & purification ; Plasminogen Activator Inhibitor 1/metabolism ; Polymers/metabolism ; Protein Conformation ; Protein Multimerization ; Protein Stability ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Sequence Analysis, Protein ; Serine Proteinase Inhibitors/chemistry ; Serine Proteinase Inhibitors/genetics ; Serine Proteinase Inhibitors/isolation & purification ; Serine Proteinase Inhibitors/metabolism ; Tandem Mass Spectrometry ; Time Factors
Chemical Substances	Plasminogen Activator Inhibitor 1 ; Polymers ; Recombinant Proteins ; Serine Proteinase Inhibitors
Language	English
Publishing date	2009-01
Publishing country	Greece
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1444428-8
ISSN	1107-3756
ISSN	1107-3756
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 4942: Show issues

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Article: Do human lipoxygenases have a PDZ regulatory domain?

Jankun, Jerzy / Doerks, Tobias / Aleem, Ansari M / Lysiak-Szydłowska, Wiesława / Skrzypczak-Jankun, Ewa

Current molecular medicine

2008 Volume 8, Issue 8, Page(s) 768–773

Abstract: Human lipoxygenases and products of their catalytic reaction have a well established connection to many human diseases. Despite their importance in inflammation, cancer, cardiorenal and other ailments the drug development is impaired by the lack of ... ...

Abstract	Human lipoxygenases and products of their catalytic reaction have a well established connection to many human diseases. Despite their importance in inflammation, cancer, cardiorenal and other ailments the drug development is impaired by the lack of structural details to understand their intricate specificity and function in molecular and cellular signaling. The major effort so far has been directed towards understanding the determinants of their specificity and inhibition of their active site with the iron cofactor. Their structure is believed to consist of only two domains: one regulatory - a beta-sandwich, important for membrane binding, and one, mostly helical, catalytic domain. Although recently published cohort studies on single nucleotide polymorphism and occurrence of diseases, SAXS analysis and new biochemical data throw new light on lipoxygenase suggesting symbiosis of regulatory functions with an allosteric mechanism and more flexible structure than anticipated. The goal of this brief review is to direct an attention to the structural features of an anticipated topology and stimulate discussion/research to prove or disapprove our hypothesis that lipoxygenases may possess about approximately 110 amino acids PDZ-like fragments of functional importance. If they do have a second regulatory domain, it might help to explain their association with other molecules, role in signaling pathways and present a new avenue to explore the regulation of their behavior, and thus intervention in the course of diseases.
MeSH term(s)	Amino Acid Sequence ; Humans ; Lipoxygenase/chemistry ; Lipoxygenase/genetics ; Lipoxygenase/metabolism ; Models, Molecular ; Molecular Sequence Data ; PDZ Domains/genetics ; Sequence Homology, Amino Acid
Chemical Substances	Lipoxygenase (EC 1.13.11.12)
Language	English
Publishing date	2008-10-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2064873-X
ISSN	1566-5240
ISSN	1566-5240
DOI	10.2174/156652408786733757
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Zs.A 5580: Show issues

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